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A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins

Author(s)
Kapila, Atul; Halfmann, Randal Arthur; Lindquist, Susan; King, Oliver D.; Alberti, Simon
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Abstract
Prions are proteins that convert between structurally and functionally distinct states, one or more of which is transmissible. In yeast, this ability allows them to act as non-Mendelian elements of phenotypic inheritance. To further our understanding of prion biology, we conducted a bioinformatic proteome-wide survey for prionogenic proteins in S. cerevisiae, followed by experimental investigations of 100 prion candidates. We found an unexpected amino acid bias in aggregation-prone candidates and discovered that 19 of these could also form prions. At least one of these prion proteins, Mot3, produces a bona fide prion in its natural context that increases population-level phenotypic heterogeneity. The self-perpetuating states of these proteins present a vast source of heritable phenotypic variation that increases the adaptability of yeast populations to diverse environments.
Date issued
2009-04
URI
http://hdl.handle.net/1721.1/54771
Department
Massachusetts Institute of Technology. Department of Biology
Journal
Cell
Publisher
Elsevier
Citation
Alberti, Simon et al. “A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins.” Cell137.1 (2009): 146-158.
Version: Author's final manuscript
ISSN
0092-8674
1097-4172

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